Amino acids, in particular L-lysine, are used in human medicine and in the pharmaceuticals industry, but in particular in animal nutrition.
It is known that amino acids are prepared by fermentation from strains of coryneform bacteria, in particular Corynebacterium glutamicum. Because of their great importance, work is constantly being undertaken to improve the preparation processes. Improvements to the processes can relate to fermentation measures, such as e.g. stirring and supply of oxygen, or the composition of the nutrient media, such as e.g. the sugar concentration during the fermentation, or the working up to the product form by e.g. ion exchange chromatography, or the intrinsic output properties of the microorganism itself.
Methods of mutagenesis, selection and mutant selection are used to improve the output properties of these microorganisms. Strains which are resistant to antimetabolites, such as e.g. the lysine analogue S-(2-aminoethyl)-cysteine, or are auxotrophic for metabolites of regulatory importance and produce L-amino acids, such as e.g. L-lysine, are obtained in this manner. Methods of the recombinant DNA technique have also been employed for some years for improving the strain of Corynebacterium strains which produce amino acids.
The importance of the pentose phosphate cycle for the biosynthesis is known.
Thus Oishi and Aida (Agricultural and Biological Chemistry 29, 83-89 (1965)) already report on the “hexose monophosphate shunt” of Brevibacterium ammoniagenes. Sugimoto and Shio (Agricultural and Biological Chemistry 51, 101-108 (1987)) report on the regulation of glucose 6-phosphate dehydrogenase in Brevibacterium flavum. Sugimoto and Shio (Agricultural and Biological Chemistry 51, 1257-11263 (1987)) report on the regulation of glucose 6-phosphate dehydrogenase in Brevibacterium flavum. 
JP-A-09224661 discloses the nucleotide sequence of the glucose 6-phosphate dehydrogenase gene, called zwf, of Brevibacterium flavum MJ-223 (FERM BP-1497). JP-A-09224661 describes the N-terminal amino acid sequence of the Zwf polypeptide as Met Val Ile Phe Gly Val Thr Gly Asp Leu Ala Arg Lys Lys Leu.
However, it has not been possible to confirm this.